Sandbox Reserved 774: Difference between revisions

Line 9:

=Structure=

Has a chain structure with 2.4 A resolution, and 2.9 A resolution with a co-factor (acetyl-CoA). The method used to determine the structure was X-ray crystallography. Sedimentation and crystal structure analysis clearly shows that Hpa2 is dimeric in solution and tetramerizes in the unit crystal. The average B-factor value is 23.9 (main chain) with a 25.4 side chain. The R-factor is 0.19. Core fold features four conserved sequence motifs of the GNAT family and comprises a central highly curved five stranded beta-sheet (β1-β5) surrounded on both sides by helical segments (α1 and α3).

Has a chain structure with 2.4 A resolution, and 2.9 A resolution with a co-factor (acetyl-CoA). The method used to determine the structure was X-ray crystallography. Sedimentation and crystal structure analysis clearly shows that Hpa2 is dimeric in solution and tetramerizes in the unit crystal. The crystal structure of the oligomer reveals that two Hpa2 dimers are held together by interaction between the bound acetyl-CoA molecules. The average B-factor value is 23.9 (main chain) with a 25.4 side chain. The R-factor is 0.19. Core fold features four conserved sequence motifs of the GNAT family and comprises a central highly curved five stranded beta-sheet (β1-β5) surrounded on both sides by helical segments (α1 and α3).

=Secondary Structure=

Most of the secondary structure elements of the monomer contribute residues involved in dimer contacts. A large part of the interface is formed by two projections from the core part of the monomer structure. The first projection is formed by the C-terminal end of strand B3, turn B3-B4, and the N-terminal end of strand B4, while the second is formed by strand B7. Together with strands B5 and B6 they form a barrel-like structure containing ten strands in which the component strands of the barrel locked together. Most importantly, strand b7 from each monomer interacts between strands b5 and b6 of the opposite monomer, which also extends the central sheet structure by two strands.

Most of the secondary structure elements of the monomer contribute residues involved in dimer contacts. A large part of the interface is formed by two projections from the core part of the monomer structure. The first projection is formed by the C-terminal end of strand B3, turn B3-B4, and the N-terminal end of strand B4, while the second is formed by strand B7. Together with strands B5 and B6 they form a barrel-like structure containing ten strands in which the component strands of the barrel locked together. Most importantly, strand b7 from each monomer interacts between strands b5 and b6 of the opposite monomer, which also extends the central sheet structure by two strands. Also, the two projections interact with residues from helices a1 and a2, turn a1 a2, turn a2 b2, and helices a3 and a4 of the opposite monomer. There are eight beta-strands, four alpha-helices, and ten turns.

Also, the two projections interact with residues from helices a1 and a2, turn a1 a2, turn a2 b2, and helices a3 and a4 of the opposite monomer. There are eight beta-strands, four alpha-helices, and ten turns.

[[Image:Hpa2_Active_Sites.jpg]]

Sandbox Reserved 774: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 9: / Line 9: @@
 =Structure=
-Has a chain structure with 2.4 A resolution, and 2.9 A resolution with a co-factor (acetyl-CoA). The method used to determine the structure was X-ray crystallography. Sedimentation and crystal structure analysis clearly shows that Hpa2 is dimeric in solution and tetramerizes in the unit crystal. The average B-factor value is 23.9 (main chain) with a 25.4 side chain. The R-factor is 0.19. Core fold features four conserved sequence motifs of the GNAT family and comprises a central highly curved five stranded beta-sheet (β1-β5) surrounded on both sides by helical segments (α1 and α3).
+Has a chain structure with 2.4 A resolution, and 2.9 A resolution with a co-factor (acetyl-CoA). The method used to determine the structure was X-ray crystallography. Sedimentation and crystal structure analysis clearly shows that Hpa2 is dimeric in solution and tetramerizes in the unit crystal. The crystal structure of the oligomer reveals that two Hpa2 dimers are held together by interaction between the bound acetyl-CoA molecules. The average B-factor value is 23.9 (main chain) with a 25.4 side chain. The R-factor is 0.19. Core fold features four conserved sequence motifs of the GNAT family and comprises a central highly curved five stranded beta-sheet (β1-β5) surrounded on both sides by helical segments (α1 and α3).
 =Secondary Structure=
-Most of the secondary structure elements of the monomer contribute residues involved in dimer contacts. A large part of the interface is formed by two projections from the core part of the monomer structure. The first projection is formed by the C-terminal end of strand B3, turn B3-B4, and the N-terminal end of strand B4, while the second is formed by strand B7. Together with strands B5 and B6 they form a barrel-like structure containing ten strands in which the component strands of the barrel locked together. Most importantly, strand b7 from each monomer interacts between strands b5 and b6 of the opposite monomer, which also extends the central sheet structure by two strands.
+Most of the secondary structure elements of the monomer contribute residues involved in dimer contacts. A large part of the interface is formed by two projections from the core part of the monomer structure. The first projection is formed by the C-terminal end of strand B3, turn B3-B4, and the N-terminal end of strand B4, while the second is formed by strand B7. Together with strands B5 and B6 they form a barrel-like structure containing ten strands in which the component strands of the barrel locked together. Most importantly, strand b7 from each monomer interacts between strands b5 and b6 of the opposite monomer, which also extends the central sheet structure by two strands. Also, the two projections interact with residues from helices a1 and a2, turn a1 a2, turn a2 b2, and helices a3 and a4 of the opposite monomer. There are eight beta-strands, four alpha-helices, and ten turns.
-Also, the two projections interact with residues from helices a1 and a2, turn a1 a2, turn a2 b2, and helices a3 and a4 of the opposite monomer. There are eight beta-strands, four alpha-helices, and ten turns.
 [[Image:Hpa2_Active_Sites.jpg]]